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Crystal structure of an rmlc-like cupin protein (REUT_A0381) from ralstonia eutropha JMP134 at 2.60 a resolution

Analyse Crystal structure of an rmlc-like cupin protein (REUT_A0381) from ralstonia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EBR
Type: protein
Length: 157 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized rmlc-like cupin
UniProt: Q476C0
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized rmlc-like cupin	protein	157	13% helix, 38% strand	Q476C0

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	311	0.82	0.92	43	PEG

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3EBR · Crystal structure of an rmlc-like cupin protein (reut_a0381) from ralstonia eutropha… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q476C0
Elsewhere: RCSB PDB 3EBR · PDBe 3EBR · UniProt Q476C0

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